Probing the Acid-Induced Packing Structure Changes of the Molten Globule Domains of a Protein near Equilibrium Unfolding
Author:
Affiliation:
1. National Synchrotron Radiation Research Center, Hsinchu 30076, Taiwan
2. Department of Chemical Engineering, National Tsing Hua University, Hsinchu 30013, Taiwan
Funder
Ministry of Science and Technology, Taiwan
Publisher
American Chemical Society (ACS)
Subject
General Materials Science,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpclett.6b02722
Reference50 articles.
1. Dry molten globule intermediates and the mechanism of protein unfolding
2. Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride
3. Evidence for Dry Molten Globule-Like Domains in the pH-Induced Equilibrium Folding Intermediate of a Multidomain Protein
4. Packing in molten globules and native states
5. Dynamic hydration shell restores Kauzmann's 1959 explanation of how the hydrophobic factor drives protein folding
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